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1ihk
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(New page: 200px<br /> <applet load="1ihk" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ihk, resolution 2.2Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 15:23, 12 November 2007
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CRYSTAL STRUCTURE OF FIBROBLAST GROWTH FACTOR 9 (FGF9)
Overview
Fibroblast growth factors (FGFs) constitute a large family of, heparin-binding growth factors with diverse biological activities. FGF9, was originally described as glia-activating factor and is expressed in the, nervous system as a potent mitogen for glia cells. Unlike most FGFs, FGF9, forms dimers in solution with a K(d) of 680 nm. To elucidate the molecular, mechanism of FGF9 dimerization, the crystal structure of FGF9 was, determined at 2.2 A resolution. FGF9 adopts a beta-trefoil fold similar to, other FGFs. However, unlike other FGFs, the N- and C-terminal regions, outside the beta-trefoil core in FGF9 are ordered and involved in the, formation of a 2-fold crystallographic dimer. A significant surface area, (>2000 A(2)) is buried in the dimer interface that occludes a major, receptor binding site of FGF9. Thus, we propose an autoinhibitory, mechanism for FGF9 that is dependent on sequences outside of the, beta-trefoil core. Moreover, a model is presented providing a molecular, basis for the preferential affinity of FGF9 toward FGFR3.
About this Structure
1IHK is a Single protein structure of sequence from Homo sapiens with PO4 as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of fibroblast growth factor 9 reveals regions implicated in dimerization and autoinhibition., Plotnikov AN, Eliseenkova AV, Ibrahimi OA, Shriver Z, Sasisekharan R, Lemmon MA, Mohammadi M, J Biol Chem. 2001 Feb 9;276(6):4322-9. Epub 2000 Nov 1. PMID:11060292
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